2FMF

Crystal structure of CheY in complex with CheZ 200-214 solved from a F432 crystal grown in Hepes (pH 7.5)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000160	biological_process	phosphorelay signal transduction system
A	0005737	cellular_component	cytoplasm
A	0006935	biological_process	chemotaxis
A	0046872	molecular_function	metal ion binding
A	0097588	biological_process	archaeal or bacterial-type flagellum-dependent cell motility

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 A 150

Chain	Residue
A	LYS70
A	LYS70
A	LYS70
A	HOH222
A	HOH222
A	HOH222

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250|UniProtKB:A0A0H3AMJ9

Chain	Residue	Details
A	ASP13

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8257674, ECO:0007744|PDB:2CHE, ECO:0007744|PDB:2FKA, ECO:0007744|PDB:2FLW, ECO:0007744|PDB:2FMH, ECO:0007744|PDB:2FMK, ECO:0007744|PDB:2PL9, ECO:0007744|PDB:2PMC

Chain	Residue	Details
A	PHE14
A	TRP58
A	MET60

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: 4-aspartylphosphate => ECO:0000255|PROSITE-ProRule:PRU00169, ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143

Chain	Residue	Details
A	TRP58

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250

Chain	Residue	Details
A	GLU93
A	PRO110

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